HEADER OXIDOREDUCTASE 18-APR-16 5JE8
TITLE THE CRYSTAL STRUCTURE OF BACILLUS CEREUS 3-HYDROXYISOBUTYRATE
TITLE 2 DEHYDROGENASE IN COMPLEX WITH NAD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-HYDROXYISOBUTYRATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.1.1.31;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS ATCC 14579;
SOURCE 3 ORGANISM_TAXID: 226900;
SOURCE 4 STRAIN: ATCC 14579;
SOURCE 5 GENE: BC_2289;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.PARK,S.I.YOON
REVDAT 3 08-NOV-23 5JE8 1 JRNL REMARK
REVDAT 2 01-JUN-16 5JE8 1 JRNL
REVDAT 1 11-MAY-16 5JE8 0
JRNL AUTH S.C.PARK,P.H.KIM,G.S.LEE,S.G.KANG,H.J.KO,S.I.YOON
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE BACILLUS
JRNL TITL 2 CEREUS 3-HYDROXYISOBUTYRATE DEHYDROGENASE
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 474 522 2016
JRNL REFN ESSN 1090-2104
JRNL PMID 27120461
JRNL DOI 10.1016/J.BBRC.2016.04.126
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 67647
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3585
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4898
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 251
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8807
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 203
REMARK 3 SOLVENT ATOMS : 561
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.84000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : -0.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.242
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9211 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6043 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12483 ; 1.483 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14915 ; 4.284 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1174 ; 5.936 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 368 ;40.631 ;25.978
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1572 ;16.605 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.639 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1431 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10189 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1751 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5769 ; 0.613 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2409 ; 0.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9237 ; 1.012 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3442 ; 1.892 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3240 ; 3.008 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 172 5
REMARK 3 2 B 3 B 172 5
REMARK 3 3 C 3 C 172 5
REMARK 3 4 D 3 D 172 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 993 ; 0.310 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 993 ; 0.160 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 993 ; 0.190 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 993 ; 0.240 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 1042 ; 0.670 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 1042 ; 0.450 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 1042 ; 0.530 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 1042 ; 0.590 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 993 ; 0.140 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 993 ; 0.180 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 993 ; 0.080 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 993 ; 0.140 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 1042 ; 0.520 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 1042 ; 0.590 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 1042 ; 0.420 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 1042 ; 0.440 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 173 A 290 5
REMARK 3 2 B 173 B 290 5
REMARK 3 3 C 173 C 290 5
REMARK 3 4 D 173 D 290 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 700 ; 0.170 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 B (A): 700 ; 0.160 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 C (A): 700 ; 0.220 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 D (A): 700 ; 0.180 ; 0.500
REMARK 3 LOOSE POSITIONAL 2 A (A): 788 ; 0.440 ; 5.000
REMARK 3 LOOSE POSITIONAL 2 B (A): 788 ; 0.350 ; 5.000
REMARK 3 LOOSE POSITIONAL 2 C (A): 788 ; 0.430 ; 5.000
REMARK 3 LOOSE POSITIONAL 2 D (A): 788 ; 0.380 ; 5.000
REMARK 3 MEDIUM THERMAL 2 A (A**2): 700 ; 4.060 ; 2.000
REMARK 3 MEDIUM THERMAL 2 B (A**2): 700 ; 4.650 ; 2.000
REMARK 3 MEDIUM THERMAL 2 C (A**2): 700 ; 2.520 ; 2.000
REMARK 3 MEDIUM THERMAL 2 D (A**2): 700 ;10.920 ; 2.000
REMARK 3 LOOSE THERMAL 2 A (A**2): 788 ; 3.650 ;10.000
REMARK 3 LOOSE THERMAL 2 B (A**2): 788 ; 4.140 ;10.000
REMARK 3 LOOSE THERMAL 2 C (A**2): 788 ; 2.510 ;10.000
REMARK 3 LOOSE THERMAL 2 D (A**2): 788 ; 9.900 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 401 A 401 5
REMARK 3 2 B 401 B 401 5
REMARK 3 3 C 401 C 401 5
REMARK 3 4 D 401 D 401 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 3 A (A): 66 ; 0.230 ; 5.000
REMARK 3 LOOSE POSITIONAL 3 B (A): 66 ; 0.180 ; 5.000
REMARK 3 LOOSE POSITIONAL 3 C (A): 66 ; 0.170 ; 5.000
REMARK 3 LOOSE POSITIONAL 3 D (A): 66 ; 0.170 ; 5.000
REMARK 3 LOOSE THERMAL 3 A (A**2): 66 ;10.070 ;10.000
REMARK 3 LOOSE THERMAL 3 B (A**2): 66 ; 3.590 ;10.000
REMARK 3 LOOSE THERMAL 3 C (A**2): 66 ;13.180 ;10.000
REMARK 3 LOOSE THERMAL 3 D (A**2): 66 ; 6.670 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 172
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7780 57.5630 23.1330
REMARK 3 T TENSOR
REMARK 3 T11: 0.2150 T22: 0.2149
REMARK 3 T33: 0.3152 T12: 0.0094
REMARK 3 T13: 0.0017 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 3.0497 L22: 2.4799
REMARK 3 L33: 1.5272 L12: 1.1537
REMARK 3 L13: -0.4044 L23: -0.8128
REMARK 3 S TENSOR
REMARK 3 S11: 0.1025 S12: -0.2185 S13: 0.1410
REMARK 3 S21: 0.1742 S22: -0.0673 S23: 0.2478
REMARK 3 S31: -0.0722 S32: -0.0101 S33: -0.0351
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 173 A 291
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5080 29.6730 18.4180
REMARK 3 T TENSOR
REMARK 3 T11: 0.1181 T22: 0.1827
REMARK 3 T33: 0.3907 T12: -0.0136
REMARK 3 T13: -0.0325 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 1.0607 L22: 2.9151
REMARK 3 L33: 1.1860 L12: 0.1728
REMARK 3 L13: -0.6200 L23: 0.0192
REMARK 3 S TENSOR
REMARK 3 S11: 0.1193 S12: -0.0816 S13: 0.0910
REMARK 3 S21: 0.1732 S22: -0.1170 S23: -0.5535
REMARK 3 S31: -0.1026 S32: 0.1498 S33: -0.0022
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -1 B 172
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7770 1.9880 -4.2580
REMARK 3 T TENSOR
REMARK 3 T11: 0.2498 T22: 0.2015
REMARK 3 T33: 0.3028 T12: 0.0240
REMARK 3 T13: 0.0392 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 1.9328 L22: 1.8453
REMARK 3 L33: 1.7313 L12: 0.3929
REMARK 3 L13: 0.7310 L23: -0.0397
REMARK 3 S TENSOR
REMARK 3 S11: 0.0482 S12: 0.0813 S13: -0.1073
REMARK 3 S21: -0.1183 S22: 0.0149 S23: -0.1261
REMARK 3 S31: 0.2171 S32: 0.0439 S33: -0.0632
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 173 B 292
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7920 22.4500 17.8060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1201 T22: 0.1708
REMARK 3 T33: 0.2669 T12: -0.0047
REMARK 3 T13: -0.0032 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.6230 L22: 2.5775
REMARK 3 L33: 0.9305 L12: 0.0838
REMARK 3 L13: -0.2668 L23: -0.1704
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: 0.0941 S13: 0.0301
REMARK 3 S21: 0.0303 S22: -0.1056 S23: 0.0650
REMARK 3 S31: 0.0307 S32: -0.0541 S33: 0.0496
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 172
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5010 -46.5850 14.1280
REMARK 3 T TENSOR
REMARK 3 T11: 0.4293 T22: 0.2591
REMARK 3 T33: 0.3452 T12: -0.1036
REMARK 3 T13: 0.0290 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 1.7290 L22: 7.8094
REMARK 3 L33: 4.0087 L12: -0.4076
REMARK 3 L13: -0.2890 L23: -2.2718
REMARK 3 S TENSOR
REMARK 3 S11: -0.1981 S12: -0.0730 S13: 0.0089
REMARK 3 S21: -0.0831 S22: 0.1282 S23: -0.2188
REMARK 3 S31: 0.2198 S32: -0.0723 S33: 0.0698
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 173 C 290
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4220 -21.6840 25.5710
REMARK 3 T TENSOR
REMARK 3 T11: 0.8319 T22: 0.1203
REMARK 3 T33: 0.3062 T12: 0.0532
REMARK 3 T13: -0.1562 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.1492 L22: 8.6307
REMARK 3 L33: 2.5695 L12: -0.2184
REMARK 3 L13: 1.0566 L23: 2.4998
REMARK 3 S TENSOR
REMARK 3 S11: -0.1515 S12: -0.0216 S13: -0.0641
REMARK 3 S21: 1.8232 S22: 0.2930 S23: -0.9025
REMARK 3 S31: 0.8944 S32: -0.0002 S33: -0.1415
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 172
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2450 9.0230 44.6290
REMARK 3 T TENSOR
REMARK 3 T11: 0.7260 T22: 0.2391
REMARK 3 T33: 0.2858 T12: -0.0578
REMARK 3 T13: 0.0202 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 2.1591 L22: 2.9706
REMARK 3 L33: 4.0151 L12: -0.5181
REMARK 3 L13: -0.0175 L23: 1.3360
REMARK 3 S TENSOR
REMARK 3 S11: 0.1452 S12: -0.1513 S13: 0.0838
REMARK 3 S21: 0.7694 S22: -0.0697 S23: -0.0090
REMARK 3 S31: 1.0280 S32: -0.1394 S33: -0.0755
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5JE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00001
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72368
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3CKY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 6000, 0.1 M HEPES, PH 7.4,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.22200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.56900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.28800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.56900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.22200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 79.28800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 ALA A -3
REMARK 465 LYS A -2
REMARK 465 ASP A -1
REMARK 465 PRO A 0
REMARK 465 ILE A 292
REMARK 465 SER A 293
REMARK 465 ASN A 294
REMARK 465 GLN A 295
REMARK 465 LYS A 296
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 ALA B -3
REMARK 465 LYS B -2
REMARK 465 SER B 293
REMARK 465 ASN B 294
REMARK 465 GLN B 295
REMARK 465 LYS B 296
REMARK 465 GLY C -5
REMARK 465 SER C -4
REMARK 465 ALA C -3
REMARK 465 LYS C -2
REMARK 465 ASP C -1
REMARK 465 PRO C 0
REMARK 465 MET C 1
REMARK 465 LEU C 291
REMARK 465 ILE C 292
REMARK 465 SER C 293
REMARK 465 ASN C 294
REMARK 465 GLN C 295
REMARK 465 LYS C 296
REMARK 465 GLY D -5
REMARK 465 SER D -4
REMARK 465 ALA D -3
REMARK 465 LYS D -2
REMARK 465 ASP D -1
REMARK 465 PRO D 0
REMARK 465 SER D 293
REMARK 465 ASN D 294
REMARK 465 GLN D 295
REMARK 465 LYS D 296
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 110 CD CE NZ
REMARK 470 LYS A 113 CE NZ
REMARK 470 LYS A 202 CG CD CE NZ
REMARK 470 GLU A 228 CG CD OE1 OE2
REMARK 470 LYS A 241 CD CE NZ
REMARK 470 GLN A 272 CD OE1 NE2
REMARK 470 ASP B -1 CG OD1 OD2
REMARK 470 MET B 1 CG SD CE
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 LYS B 110 CE NZ
REMARK 470 ILE B 292 CG1 CG2 CD1
REMARK 470 ARG C 69 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 107 CG CD OE1 OE2
REMARK 470 LYS C 146 CE NZ
REMARK 470 ASP C 201 CG OD1 OD2
REMARK 470 ASN C 229 CG OD1 ND2
REMARK 470 LYS C 285 CG CD CE NZ
REMARK 470 GLU C 289 CG CD OE1 OE2
REMARK 470 GLN C 290 CG CD OE1 NE2
REMARK 470 MET D 1 CG SD CE
REMARK 470 GLU D 35 OE1 OE2
REMARK 470 GLU D 79 OE1 OE2
REMARK 470 LYS D 112 NZ
REMARK 470 LYS D 141 CG CD CE NZ
REMARK 470 ASP D 142 CG OD1 OD2
REMARK 470 LYS D 146 CD CE NZ
REMARK 470 ILE D 150 CD1
REMARK 470 LYS D 202 CG CD CE NZ
REMARK 470 ARG D 215 NE CZ NH1 NH2
REMARK 470 GLU D 231 OE1 OE2
REMARK 470 ILE D 292 CG1 CG2 CD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 224 -59.05 -136.57
REMARK 500 MET B 1 59.96 -143.81
REMARK 500 LEU B 9 46.77 -108.02
REMARK 500 PHE B 224 -66.38 -132.09
REMARK 500 LEU C 9 53.89 -111.15
REMARK 500 GLU C 43 32.64 -96.17
REMARK 500 SER C 210 -168.40 -109.00
REMARK 500 PHE C 224 -51.98 -134.35
REMARK 500 LEU D 9 47.90 -104.89
REMARK 500 SER D 210 -168.79 -124.04
REMARK 500 PHE D 224 -52.68 -126.32
REMARK 500 PRO D 227 2.57 -68.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402
DBREF 5JE8 A 1 296 UNP Q81DR6 Q81DR6_BACCR 1 296
DBREF 5JE8 B 1 296 UNP Q81DR6 Q81DR6_BACCR 1 296
DBREF 5JE8 C 1 296 UNP Q81DR6 Q81DR6_BACCR 1 296
DBREF 5JE8 D 1 296 UNP Q81DR6 Q81DR6_BACCR 1 296
SEQADV 5JE8 GLY A -5 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 SER A -4 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ALA A -3 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 LYS A -2 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ASP A -1 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 PRO A 0 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 GLY B -5 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 SER B -4 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ALA B -3 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 LYS B -2 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ASP B -1 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 PRO B 0 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 GLY C -5 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 SER C -4 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ALA C -3 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 LYS C -2 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ASP C -1 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 PRO C 0 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 GLY D -5 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 SER D -4 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ALA D -3 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 LYS D -2 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 ASP D -1 UNP Q81DR6 EXPRESSION TAG
SEQADV 5JE8 PRO D 0 UNP Q81DR6 EXPRESSION TAG
SEQRES 1 A 302 GLY SER ALA LYS ASP PRO MET LYS LYS ILE GLY PHE ILE
SEQRES 2 A 302 GLY LEU GLY ASN MET GLY LEU PRO MET SER LYS ASN LEU
SEQRES 3 A 302 VAL LYS SER GLY TYR THR VAL TYR GLY VAL ASP LEU ASN
SEQRES 4 A 302 LYS GLU ALA GLU ALA SER PHE GLU LYS GLU GLY GLY ILE
SEQRES 5 A 302 ILE GLY LEU SER ILE SER LYS LEU ALA GLU THR CYS ASP
SEQRES 6 A 302 VAL VAL PHE THR SER LEU PRO SER PRO ARG ALA VAL GLU
SEQRES 7 A 302 ALA VAL TYR PHE GLY ALA GLU GLY LEU PHE GLU ASN GLY
SEQRES 8 A 302 HIS SER ASN VAL VAL PHE ILE ASP THR SER THR VAL SER
SEQRES 9 A 302 PRO GLN LEU ASN LYS GLN LEU GLU GLU ALA ALA LYS GLU
SEQRES 10 A 302 LYS LYS VAL ASP PHE LEU ALA ALA PRO VAL SER GLY GLY
SEQRES 11 A 302 VAL ILE GLY ALA GLU ASN ARG THR LEU THR PHE MET VAL
SEQRES 12 A 302 GLY GLY SER LYS ASP VAL TYR GLU LYS THR GLU SER ILE
SEQRES 13 A 302 MET GLY VAL LEU GLY ALA ASN ILE PHE HIS VAL SER GLU
SEQRES 14 A 302 GLN ILE ASP SER GLY THR THR VAL LYS LEU ILE ASN ASN
SEQRES 15 A 302 LEU LEU ILE GLY PHE TYR THR ALA GLY VAL SER GLU ALA
SEQRES 16 A 302 LEU THR LEU ALA LYS LYS ASN ASN MET ASP LEU ASP LYS
SEQRES 17 A 302 MET PHE ASP ILE LEU ASN VAL SER TYR GLY GLN SER ARG
SEQRES 18 A 302 ILE TYR GLU ARG ASN TYR LYS SER PHE ILE ALA PRO GLU
SEQRES 19 A 302 ASN TYR GLU PRO GLY PHE THR VAL ASN LEU LEU LYS LYS
SEQRES 20 A 302 ASP LEU GLY PHE ALA VAL ASP LEU ALA LYS GLU SER GLU
SEQRES 21 A 302 LEU HIS LEU PRO VAL SER GLU MET LEU LEU ASN VAL TYR
SEQRES 22 A 302 ASP GLU ALA SER GLN ALA GLY TYR GLY GLU ASN ASP MET
SEQRES 23 A 302 ALA ALA LEU TYR LYS LYS VAL SER GLU GLN LEU ILE SER
SEQRES 24 A 302 ASN GLN LYS
SEQRES 1 B 302 GLY SER ALA LYS ASP PRO MET LYS LYS ILE GLY PHE ILE
SEQRES 2 B 302 GLY LEU GLY ASN MET GLY LEU PRO MET SER LYS ASN LEU
SEQRES 3 B 302 VAL LYS SER GLY TYR THR VAL TYR GLY VAL ASP LEU ASN
SEQRES 4 B 302 LYS GLU ALA GLU ALA SER PHE GLU LYS GLU GLY GLY ILE
SEQRES 5 B 302 ILE GLY LEU SER ILE SER LYS LEU ALA GLU THR CYS ASP
SEQRES 6 B 302 VAL VAL PHE THR SER LEU PRO SER PRO ARG ALA VAL GLU
SEQRES 7 B 302 ALA VAL TYR PHE GLY ALA GLU GLY LEU PHE GLU ASN GLY
SEQRES 8 B 302 HIS SER ASN VAL VAL PHE ILE ASP THR SER THR VAL SER
SEQRES 9 B 302 PRO GLN LEU ASN LYS GLN LEU GLU GLU ALA ALA LYS GLU
SEQRES 10 B 302 LYS LYS VAL ASP PHE LEU ALA ALA PRO VAL SER GLY GLY
SEQRES 11 B 302 VAL ILE GLY ALA GLU ASN ARG THR LEU THR PHE MET VAL
SEQRES 12 B 302 GLY GLY SER LYS ASP VAL TYR GLU LYS THR GLU SER ILE
SEQRES 13 B 302 MET GLY VAL LEU GLY ALA ASN ILE PHE HIS VAL SER GLU
SEQRES 14 B 302 GLN ILE ASP SER GLY THR THR VAL LYS LEU ILE ASN ASN
SEQRES 15 B 302 LEU LEU ILE GLY PHE TYR THR ALA GLY VAL SER GLU ALA
SEQRES 16 B 302 LEU THR LEU ALA LYS LYS ASN ASN MET ASP LEU ASP LYS
SEQRES 17 B 302 MET PHE ASP ILE LEU ASN VAL SER TYR GLY GLN SER ARG
SEQRES 18 B 302 ILE TYR GLU ARG ASN TYR LYS SER PHE ILE ALA PRO GLU
SEQRES 19 B 302 ASN TYR GLU PRO GLY PHE THR VAL ASN LEU LEU LYS LYS
SEQRES 20 B 302 ASP LEU GLY PHE ALA VAL ASP LEU ALA LYS GLU SER GLU
SEQRES 21 B 302 LEU HIS LEU PRO VAL SER GLU MET LEU LEU ASN VAL TYR
SEQRES 22 B 302 ASP GLU ALA SER GLN ALA GLY TYR GLY GLU ASN ASP MET
SEQRES 23 B 302 ALA ALA LEU TYR LYS LYS VAL SER GLU GLN LEU ILE SER
SEQRES 24 B 302 ASN GLN LYS
SEQRES 1 C 302 GLY SER ALA LYS ASP PRO MET LYS LYS ILE GLY PHE ILE
SEQRES 2 C 302 GLY LEU GLY ASN MET GLY LEU PRO MET SER LYS ASN LEU
SEQRES 3 C 302 VAL LYS SER GLY TYR THR VAL TYR GLY VAL ASP LEU ASN
SEQRES 4 C 302 LYS GLU ALA GLU ALA SER PHE GLU LYS GLU GLY GLY ILE
SEQRES 5 C 302 ILE GLY LEU SER ILE SER LYS LEU ALA GLU THR CYS ASP
SEQRES 6 C 302 VAL VAL PHE THR SER LEU PRO SER PRO ARG ALA VAL GLU
SEQRES 7 C 302 ALA VAL TYR PHE GLY ALA GLU GLY LEU PHE GLU ASN GLY
SEQRES 8 C 302 HIS SER ASN VAL VAL PHE ILE ASP THR SER THR VAL SER
SEQRES 9 C 302 PRO GLN LEU ASN LYS GLN LEU GLU GLU ALA ALA LYS GLU
SEQRES 10 C 302 LYS LYS VAL ASP PHE LEU ALA ALA PRO VAL SER GLY GLY
SEQRES 11 C 302 VAL ILE GLY ALA GLU ASN ARG THR LEU THR PHE MET VAL
SEQRES 12 C 302 GLY GLY SER LYS ASP VAL TYR GLU LYS THR GLU SER ILE
SEQRES 13 C 302 MET GLY VAL LEU GLY ALA ASN ILE PHE HIS VAL SER GLU
SEQRES 14 C 302 GLN ILE ASP SER GLY THR THR VAL LYS LEU ILE ASN ASN
SEQRES 15 C 302 LEU LEU ILE GLY PHE TYR THR ALA GLY VAL SER GLU ALA
SEQRES 16 C 302 LEU THR LEU ALA LYS LYS ASN ASN MET ASP LEU ASP LYS
SEQRES 17 C 302 MET PHE ASP ILE LEU ASN VAL SER TYR GLY GLN SER ARG
SEQRES 18 C 302 ILE TYR GLU ARG ASN TYR LYS SER PHE ILE ALA PRO GLU
SEQRES 19 C 302 ASN TYR GLU PRO GLY PHE THR VAL ASN LEU LEU LYS LYS
SEQRES 20 C 302 ASP LEU GLY PHE ALA VAL ASP LEU ALA LYS GLU SER GLU
SEQRES 21 C 302 LEU HIS LEU PRO VAL SER GLU MET LEU LEU ASN VAL TYR
SEQRES 22 C 302 ASP GLU ALA SER GLN ALA GLY TYR GLY GLU ASN ASP MET
SEQRES 23 C 302 ALA ALA LEU TYR LYS LYS VAL SER GLU GLN LEU ILE SER
SEQRES 24 C 302 ASN GLN LYS
SEQRES 1 D 302 GLY SER ALA LYS ASP PRO MET LYS LYS ILE GLY PHE ILE
SEQRES 2 D 302 GLY LEU GLY ASN MET GLY LEU PRO MET SER LYS ASN LEU
SEQRES 3 D 302 VAL LYS SER GLY TYR THR VAL TYR GLY VAL ASP LEU ASN
SEQRES 4 D 302 LYS GLU ALA GLU ALA SER PHE GLU LYS GLU GLY GLY ILE
SEQRES 5 D 302 ILE GLY LEU SER ILE SER LYS LEU ALA GLU THR CYS ASP
SEQRES 6 D 302 VAL VAL PHE THR SER LEU PRO SER PRO ARG ALA VAL GLU
SEQRES 7 D 302 ALA VAL TYR PHE GLY ALA GLU GLY LEU PHE GLU ASN GLY
SEQRES 8 D 302 HIS SER ASN VAL VAL PHE ILE ASP THR SER THR VAL SER
SEQRES 9 D 302 PRO GLN LEU ASN LYS GLN LEU GLU GLU ALA ALA LYS GLU
SEQRES 10 D 302 LYS LYS VAL ASP PHE LEU ALA ALA PRO VAL SER GLY GLY
SEQRES 11 D 302 VAL ILE GLY ALA GLU ASN ARG THR LEU THR PHE MET VAL
SEQRES 12 D 302 GLY GLY SER LYS ASP VAL TYR GLU LYS THR GLU SER ILE
SEQRES 13 D 302 MET GLY VAL LEU GLY ALA ASN ILE PHE HIS VAL SER GLU
SEQRES 14 D 302 GLN ILE ASP SER GLY THR THR VAL LYS LEU ILE ASN ASN
SEQRES 15 D 302 LEU LEU ILE GLY PHE TYR THR ALA GLY VAL SER GLU ALA
SEQRES 16 D 302 LEU THR LEU ALA LYS LYS ASN ASN MET ASP LEU ASP LYS
SEQRES 17 D 302 MET PHE ASP ILE LEU ASN VAL SER TYR GLY GLN SER ARG
SEQRES 18 D 302 ILE TYR GLU ARG ASN TYR LYS SER PHE ILE ALA PRO GLU
SEQRES 19 D 302 ASN TYR GLU PRO GLY PHE THR VAL ASN LEU LEU LYS LYS
SEQRES 20 D 302 ASP LEU GLY PHE ALA VAL ASP LEU ALA LYS GLU SER GLU
SEQRES 21 D 302 LEU HIS LEU PRO VAL SER GLU MET LEU LEU ASN VAL TYR
SEQRES 22 D 302 ASP GLU ALA SER GLN ALA GLY TYR GLY GLU ASN ASP MET
SEQRES 23 D 302 ALA ALA LEU TYR LYS LYS VAL SER GLU GLN LEU ILE SER
SEQRES 24 D 302 ASN GLN LYS
HET NAD A 401 44
HET EPE A 402 15
HET NAD B 401 44
HET GOL B 402 6
HET NAD C 401 44
HET NAD D 401 44
HET GOL D 402 6
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN EPE HEPES
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 6 EPE C8 H18 N2 O4 S
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 12 HOH *561(H2 O)
HELIX 1 AA1 MET A 12 SER A 23 1 12
HELIX 2 AA2 ASN A 33 GLU A 43 1 11
HELIX 3 AA3 SER A 50 CYS A 58 1 9
HELIX 4 AA4 SER A 67 PHE A 76 1 10
HELIX 5 AA5 GLY A 80 GLY A 85 1 6
HELIX 6 AA6 SER A 98 LYS A 113 1 16
HELIX 7 AA7 GLY A 123 ASN A 130 1 8
HELIX 8 AA8 SER A 140 GLY A 152 1 13
HELIX 9 AA9 ASP A 166 ASN A 196 1 31
HELIX 10 AB1 ASP A 199 ASN A 208 1 10
HELIX 11 AB2 SER A 214 PHE A 224 1 11
HELIX 12 AB3 THR A 235 SER A 253 1 19
HELIX 13 AB4 LEU A 257 ALA A 273 1 17
HELIX 14 AB5 ASP A 279 ALA A 281 5 3
HELIX 15 AB6 ALA A 282 GLU A 289 1 8
HELIX 16 AB7 MET B 12 SER B 23 1 12
HELIX 17 AB8 ASN B 33 GLU B 43 1 11
HELIX 18 AB9 SER B 50 CYS B 58 1 9
HELIX 19 AC1 SER B 67 PHE B 76 1 10
HELIX 20 AC2 GLY B 80 GLY B 85 1 6
HELIX 21 AC3 SER B 98 LYS B 113 1 16
HELIX 22 AC4 GLY B 123 ASN B 130 1 8
HELIX 23 AC5 SER B 140 LEU B 154 1 15
HELIX 24 AC6 ASP B 166 ASN B 196 1 31
HELIX 25 AC7 ASP B 199 ASN B 208 1 10
HELIX 26 AC8 SER B 214 PHE B 224 1 11
HELIX 27 AC9 THR B 235 SER B 253 1 19
HELIX 28 AD1 LEU B 257 ALA B 273 1 17
HELIX 29 AD2 ASP B 279 ALA B 281 5 3
HELIX 30 AD3 ALA B 282 GLU B 289 1 8
HELIX 31 AD4 MET C 12 SER C 23 1 12
HELIX 32 AD5 ASN C 33 GLU C 43 1 11
HELIX 33 AD6 SER C 50 CYS C 58 1 9
HELIX 34 AD7 SER C 67 PHE C 76 1 10
HELIX 35 AD8 GLY C 80 GLY C 85 1 6
HELIX 36 AD9 SER C 98 LYS C 113 1 16
HELIX 37 AE1 GLY C 123 ARG C 131 1 9
HELIX 38 AE2 SER C 140 LEU C 154 1 15
HELIX 39 AE3 ASP C 166 ASN C 196 1 31
HELIX 40 AE4 ASP C 199 ASN C 208 1 10
HELIX 41 AE5 SER C 214 PHE C 224 1 11
HELIX 42 AE6 THR C 235 SER C 253 1 19
HELIX 43 AE7 LEU C 257 ALA C 273 1 17
HELIX 44 AE8 ASP C 279 ALA C 281 5 3
HELIX 45 AE9 ALA C 282 GLN C 290 1 9
HELIX 46 AF1 MET D 12 SER D 23 1 12
HELIX 47 AF2 ASN D 33 GLY D 44 1 12
HELIX 48 AF3 SER D 50 CYS D 58 1 9
HELIX 49 AF4 SER D 67 PHE D 76 1 10
HELIX 50 AF5 GLY D 80 GLY D 85 1 6
HELIX 51 AF6 SER D 98 LYS D 113 1 16
HELIX 52 AF7 GLY D 123 ARG D 131 1 9
HELIX 53 AF8 SER D 140 VAL D 153 1 14
HELIX 54 AF9 ASP D 166 ASN D 196 1 31
HELIX 55 AG1 ASP D 199 VAL D 209 1 11
HELIX 56 AG2 SER D 214 PHE D 224 1 11
HELIX 57 AG3 THR D 235 SER D 253 1 19
HELIX 58 AG4 LEU D 257 ALA D 273 1 17
HELIX 59 AG5 ASP D 279 ALA D 281 5 3
HELIX 60 AG6 ALA D 282 SER D 288 1 7
HELIX 61 AG7 GLU D 289 LEU D 291 5 3
SHEET 1 AA1 5 THR A 26 VAL A 30 0
SHEET 2 AA1 5 LYS A 3 ILE A 7 1 N ILE A 4 O TYR A 28
SHEET 3 AA1 5 VAL A 60 THR A 63 1 O PHE A 62 N GLY A 5
SHEET 4 AA1 5 VAL A 90 ASP A 93 1 O VAL A 90 N VAL A 61
SHEET 5 AA1 5 ASP A 115 ALA A 118 1 O ASP A 115 N PHE A 91
SHEET 1 AA2 3 VAL A 121 SER A 122 0
SHEET 2 AA2 3 LEU A 133 GLY A 138 -1 O THR A 134 N SER A 122
SHEET 3 AA2 3 GLY A 155 SER A 162 1 O PHE A 159 N PHE A 135
SHEET 1 AA3 7 THR B 26 VAL B 30 0
SHEET 2 AA3 7 LYS B 3 ILE B 7 1 N ILE B 4 O THR B 26
SHEET 3 AA3 7 VAL B 60 THR B 63 1 O VAL B 60 N GLY B 5
SHEET 4 AA3 7 VAL B 90 ASP B 93 1 O ILE B 92 N VAL B 61
SHEET 5 AA3 7 ASP B 115 ALA B 118 1 O ASP B 115 N PHE B 91
SHEET 6 AA3 7 LEU B 133 GLY B 139 -1 O GLY B 138 N ALA B 118
SHEET 7 AA3 7 VAL B 121 SER B 122 -1 N SER B 122 O THR B 134
SHEET 1 AA4 7 THR B 26 VAL B 30 0
SHEET 2 AA4 7 LYS B 3 ILE B 7 1 N ILE B 4 O THR B 26
SHEET 3 AA4 7 VAL B 60 THR B 63 1 O VAL B 60 N GLY B 5
SHEET 4 AA4 7 VAL B 90 ASP B 93 1 O ILE B 92 N VAL B 61
SHEET 5 AA4 7 ASP B 115 ALA B 118 1 O ASP B 115 N PHE B 91
SHEET 6 AA4 7 LEU B 133 GLY B 139 -1 O GLY B 138 N ALA B 118
SHEET 7 AA4 7 GLY B 155 SER B 162 1 O PHE B 159 N VAL B 137
SHEET 1 AA5 7 VAL C 27 VAL C 30 0
SHEET 2 AA5 7 ILE C 4 ILE C 7 1 N ILE C 4 O TYR C 28
SHEET 3 AA5 7 VAL C 60 THR C 63 1 O VAL C 60 N GLY C 5
SHEET 4 AA5 7 VAL C 90 ASP C 93 1 O VAL C 90 N VAL C 61
SHEET 5 AA5 7 ASP C 115 ALA C 118 1 O LEU C 117 N ASP C 93
SHEET 6 AA5 7 LEU C 133 GLY C 139 -1 O GLY C 138 N ALA C 118
SHEET 7 AA5 7 VAL C 121 SER C 122 -1 N SER C 122 O THR C 134
SHEET 1 AA6 7 VAL C 27 VAL C 30 0
SHEET 2 AA6 7 ILE C 4 ILE C 7 1 N ILE C 4 O TYR C 28
SHEET 3 AA6 7 VAL C 60 THR C 63 1 O VAL C 60 N GLY C 5
SHEET 4 AA6 7 VAL C 90 ASP C 93 1 O VAL C 90 N VAL C 61
SHEET 5 AA6 7 ASP C 115 ALA C 118 1 O LEU C 117 N ASP C 93
SHEET 6 AA6 7 LEU C 133 GLY C 139 -1 O GLY C 138 N ALA C 118
SHEET 7 AA6 7 GLY C 155 SER C 162 1 O PHE C 159 N VAL C 137
SHEET 1 AA7 5 THR D 26 VAL D 30 0
SHEET 2 AA7 5 LYS D 3 ILE D 7 1 N ILE D 4 O TYR D 28
SHEET 3 AA7 5 VAL D 60 THR D 63 1 O PHE D 62 N GLY D 5
SHEET 4 AA7 5 VAL D 90 ASP D 93 1 O VAL D 90 N VAL D 61
SHEET 5 AA7 5 ASP D 115 ALA D 118 1 O ASP D 115 N PHE D 91
SHEET 1 AA8 3 VAL D 121 SER D 122 0
SHEET 2 AA8 3 LEU D 133 GLY D 138 -1 O THR D 134 N SER D 122
SHEET 3 AA8 3 GLY D 155 SER D 162 1 O VAL D 161 N VAL D 137
CISPEP 1 PRO A 232 GLY A 233 0 3.45
CISPEP 2 PRO B 232 GLY B 233 0 0.56
CISPEP 3 PRO C 232 GLY C 233 0 -7.04
CISPEP 4 PRO D 232 GLY D 233 0 -4.18
SITE 1 AC1 28 GLY A 10 ASN A 11 MET A 12 ASP A 31
SITE 2 AC1 28 LEU A 32 SER A 64 LEU A 65 PRO A 66
SITE 3 AC1 28 ALA A 70 VAL A 74 SER A 95 THR A 96
SITE 4 AC1 28 VAL A 121 GLY A 124 PHE A 234 LEU A 238
SITE 5 AC1 28 EPE A 402 HOH A 510 HOH A 518 HOH A 541
SITE 6 AC1 28 HOH A 574 HOH A 580 HOH A 593 HOH A 596
SITE 7 AC1 28 HOH A 599 HOH A 601 HOH A 602 HOH A 603
SITE 1 AC2 14 SER A 122 GLY A 123 GLY A 124 ILE A 126
SITE 2 AC2 14 LYS A 172 ASN A 176 ILE A 179 ARG A 219
SITE 3 AC2 14 PHE A 234 NAD A 401 HOH A 508 HOH A 514
SITE 4 AC2 14 HOH A 617 TYR B 211
SITE 1 AC3 27 GLY B 8 GLY B 10 ASN B 11 MET B 12
SITE 2 AC3 27 ASP B 31 LEU B 32 SER B 64 LEU B 65
SITE 3 AC3 27 PRO B 66 VAL B 74 SER B 95 THR B 96
SITE 4 AC3 27 VAL B 121 GLY B 124 LEU B 238 HOH B 502
SITE 5 AC3 27 HOH B 507 HOH B 508 HOH B 517 HOH B 538
SITE 6 AC3 27 HOH B 547 HOH B 570 HOH B 577 HOH B 642
SITE 7 AC3 27 GLN D 272 ALA D 273 HOH D 521
SITE 1 AC4 8 ASP B 268 SER B 271 GLN B 272 HOH B 522
SITE 2 AC4 8 HOH B 554 HOH B 597 ASN D 237 LYS D 241
SITE 1 AC5 16 GLY C 8 GLY C 10 ASN C 11 MET C 12
SITE 2 AC5 16 ASP C 31 LEU C 32 LEU C 65 PRO C 66
SITE 3 AC5 16 VAL C 74 THR C 96 VAL C 121 GLY C 124
SITE 4 AC5 16 LEU C 238 HOH C 511 HOH C 528 HOH C 538
SITE 1 AC6 17 ALA B 273 HOH B 535 GLY D 10 ASN D 11
SITE 2 AC6 17 MET D 12 ASP D 31 LEU D 32 LEU D 65
SITE 3 AC6 17 PRO D 66 SER D 95 THR D 96 VAL D 121
SITE 4 AC6 17 LEU D 238 HOH D 502 HOH D 506 HOH D 524
SITE 5 AC6 17 HOH D 562
SITE 1 AC7 8 ASN B 237 LYS B 241 HOH B 552 ASP D 268
SITE 2 AC7 8 SER D 271 GLN D 272 HOH D 512 HOH D 533
CRYST1 46.444 158.576 163.138 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021531 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006306 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
